Evidence map›Paper›PMID 17251299›Full record

ArticleJournal of virology2007

Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNA polymerase.

Laura L Marcotte, Amanda B Wass, David W Gohara, Harsh B Pathak, Jamie J Arnold, David J Filman, Craig E Cameron, James M Hogle

Abstract read
In one paragraph

Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

73 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Journal of virology · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Non-lytic spread of poliovirus requires the nonstructural protein 3CD.bioRxiv : the preprint server for biology · 2024
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

13 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Laura L MarcotteDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
Amanda B Wass
David W Gohara
Harsh B Pathak
Jamie J Arnold
David J Filman
Craig E Cameron
James M Hogle

Funding

Structural Analysis of Enterovirus Cell Entry PathwaysR01AI020566 · NIAID · SCRIPPS RESEARCH INSTITUTE · PI HOGLE, JAMES M · 1985 to 2018
$9.0M
Picornavirus Genome ReplicationR01AI053531 · NIAID · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI CAMERON, CRAIG E. · 2003 to 2017
$5.7M
Picornavirus Genome ReplicationR37AI053531 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CRAIG E. CAMERON · 2018 to 2026
$4.8M
HIGH-RESOLUTION CRYSTALLOGRAPHIC STUDIES OF POLIOVIRUSR37AI020566 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HOGLE, JAMES M · 1992 to 2001
$934k
Picornavirus Genome ReplicationR56AI053531 · NIAID · PENNSYLVANIA STATE UNIVERSITY, THE · PI CAMERON, CRAIG E. · 2008 to 2008
$439k
Structual Analysis of Enterovirus Cell Entry PathwaysR21AI020566 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HOGLE, JAMES M · 2002 to 2002
$258k
NIAID NIH HHS AI 053531NIAID NIH HHS AI 20566NIAID NIH HHS R01 AI020566NIAID NIH HHS R01 AI053531NIAID NIH HHS R21 AI020566NIAID NIH HHS R37 AI020566NIAID NIH HHS R37 AI053531NIAID NIH HHS R56 AI053531
6 · The paper itself

Abstract

Poliovirus 3CD is a multifunctional protein that serves as a precursor to the protease 3C(pro) and the viral polymerase 3D(pol) and also plays a role in the control of viral replication. Although 3CD is a fully functional protease, it lacks polymerase activity. We have solved the crystal structures of 3CD at a 3.4-A resolution and the G64S fidelity mutant of 3D(pol) at a 3.0-A resolution. In the 3CD structure, the 3C and 3D domains are joined by a poorly ordered polypeptide linker, possibly to facilitate its cleavage, in an arrangement that precludes intramolecular proteolysis. The polymerase active site is intact in both the 3CD and the 3D(pol) G64S structures, despite the disruption of a network proposed to position key residues in the active site. Therefore, changes in molecular flexibility may be responsible for the differences in fidelity and polymerase activities. Extensive packing contacts between symmetry-related 3CD molecules and the approach of the 3C domain's N terminus to the VPg binding site suggest how 3D(pol) makes biologically relevant interactions with the 3C, 3CD, and 3BCD proteins that control the uridylylation of VPg during the initiation of viral replication. Indeed, mutations designed to disrupt these interfaces have pronounced effects on the uridylylation reaction in vitro.

Indexed as

3C Viral ProteasesCrystallography, X-RayCysteine EndopeptidasesGlycineHydrogen BondingModels, MolecularMutationPoliovirusProtein BindingProtein PrecursorsProtein Structure, QuaternaryProtein Structure, TertiaryRNA-Dependent RNA PolymeraseUridineViral Proteins3C Viral ProteasesCysteine EndopeptidasesGlycineProtein PrecursorsRNA-Dependent RNA PolymeraseUridineViral Proteins

Identifiers

PMID17251299
PMCPMC1866080

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.